2IV9: B2-appendage from AP2

B2-appendage from AP2 in complex with Eps15 peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 13 Mar 2007.

Method: X-ray diffraction
Resolution: 1.9 Å
Organisms: HOMO SAPIENS, RATTUS NORVEGICUS
Chains: 3
Atoms: 4,093
Mol. weight: 55.35 kDa
Released: 13 Mar 2007

Explore 2IV9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IV9 contains 18 α-helices and 38 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	709-711	3
β-strand	712-715	4	1
α-helix	717-719	3
β-strand	723-732	10	1
β-strand	735-744	10	1
β-strand	750	1	2
β-strand	754-757	4	3
β-strand	760	1	4
β-strand	765-766	2	1
β-strand	776	1	2
β-strand	781-789	9	1
β-strand	794	1	4
β-strand	802-808	7	3
β-strand	813-819	7	3
α-helix	822-825	4
β-strand	826	1	5
α-helix	834-843	10
β-strand	850-855	6	6
α-helix	861-869	9
β-strand	874-881	8	6
β-strand	884-892	9	6
β-strand	893	1	5
β-strand	898-905	8	6
β-strand	911-917	7	6
α-helix	921-923	3
α-helix	924-936	13

Chain B: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	709-711	3
β-strand	712-715	4	7
α-helix	717-719	3
β-strand	723-732	10	7
β-strand	735-744	10	7
β-strand	750	1	8
β-strand	754-757	4	9
β-strand	760	1	10
β-strand	765-766	2	7
α-helix	775	1
β-strand	776	1	8
α-helix	777	1
β-strand	781-789	9	7
β-strand	794	1	10
β-strand	802-808	7	9
β-strand	813-819	7	9
α-helix	822-825	4
β-strand	826	1	11
α-helix	834-843	10
α-helix	846-848	3
β-strand	850-854	5	12
α-helix	861-869	9
β-strand	874-881	8	12
β-strand	884-892	9	12
β-strand	893	1	11
β-strand	898-905	8	12
β-strand	912-917	6	12
α-helix	921-923	3
α-helix	924-935	12

Chain P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	5-8	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ap-2 complex subunit beta-2	A, B	protein	238	HOMO SAPIENS	P63010 (AlphaFold model)
Epidermal growth factor receptor substrate 15 isoform B	P	protein	12	RATTUS NORVEGICUS	P42566 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2IV9_1 AP-2 COMPLEX SUBUNIT BETA-2 (chains A, B)
IGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNK
NSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCL
IPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKR
NVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN

Sequence of entity 2 (P), FASTA

>2IV9_2 EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15 ISOFORM B (chains P)
SFGDGFADFSTL

Primary citation

Role of the Ap2 Beta-Appendage Hub in Recruiting Partners for Clathrin-Coated Vesicle Assembly. Schmid, E.M., Ford, M.G.J., Burtey, A. et al. PLoS Biol (2006) 4:262. DOI 10.1371/JOURNAL.PBIO.0040262 · PubMed

Other PDB entries of the same protein (UniProt P63010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2G30 1.6 Å, beta appendage of AP2 complexed with ARH peptide
1E42 1.7 Å, Beta2-adaptin appendage domain, from clathrin adaptor AP2
5M5R 1.76 Å, Clathrin heavy chain N-terminal domain bound to beta2 adaptin clathrin box motif
6QH5 2.56 Å, AP2 clathrin adaptor mu2T156-phosphorylated core in closed conformation
2VGL 2.6 Å, AP2 clathrin adaptor core
4UQI 2.79 Å, AP2 controls clathrin polymerization with a membrane-activated switch
2IV8 2.8 Å, beta appendage in complex with b-arrestin peptide
7OHO 2.88 Å, Crystal structure of AP2 FCHO2 chimera
2JKR 2.98 Å, AP2 CLATHRIN ADAPTOR CORE with Dileucine peptide RM(phosphoS)QIKRLLSE
6URI 3.0 Å, HIV-1 Nef in complex with the CD4 cytoplasmic domain and the AP2 clathrin adaptor complex
2XA7 3.1 Å, AP2 clathrin adaptor core in active complex with cargo peptides
7OG1 3.25 Å, AP2 clathrin adaptor core in complex with cargo peptide and FCHO2

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